the Thermoproteus tenax trehalose-6-phosphate synthase/phosphatase (TPSP) exhibits high phosphatase activity, but requires activation by the co-expressed glycosyltransferase for bifunctional synthase/phosphatase activity. The glycosyltransferase mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the TPSP enzyme. Activation is mediated by complex-formation in vivo
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide. Heparin helps to retain both stability and activity of the final purified enzyme
when pyrimidine sugar nucleotides are used as substrates, there is an almost absolute requirement for a high molecular weight polyanion for activity. When the purine sugar nucleotides are used as substrates fairly good enzymatic activity is observed in absence of a polyanion, this activity increases 2 to 4fold in the presence of optimum concentrations of polyanion. Activation by the polyanion is inhibited by high salt concentrations as well as by high concentrations of mononucleoside phosphates
the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae
the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae
2.4.1.15 alpha,alpha-trehalose-phosphate synthase (UDP-forming)
results (
results (
top
